Advanced

Common Interactions between S100A4 and S100A9 Defined by a Novel Chemical Probe.

Björkman, Per LU ; Källberg, Eva LU ; Wellmar, Ulf ; Riva, Matteo LU ; Olsson, Anders LU ; He, Zhifei LU ; Törngren, Marie ; Liberg, David LU ; Ivars, Fredrik LU and Leanderson, Tomas LU (2013) In PLoS ONE 8(5).
Abstract
S100A4 and S100A9 proteins have been described as playing roles in the control of tumor growth and metastasis. We show here that a chemical probe, oxyclozanide (OX), selected for inhibiting the interaction between S100A9 and the receptor for advanced glycation end-products (RAGE) interacts with both S100A9 and S100A4. Furthermore, we show that S100A9 and S100A4 interact with RAGE and TLR4; interactions that can be inhibited by OX. Hence, S100A4 and S100A9 display similar functional elements despite their primary sequence diversity. This was further confirmed by showing that S100A4 and S100A9 dimerize both in vitro and in vivo. All of these interactions required levels of Zn(++) that are found in the extracellular space but not... (More)
S100A4 and S100A9 proteins have been described as playing roles in the control of tumor growth and metastasis. We show here that a chemical probe, oxyclozanide (OX), selected for inhibiting the interaction between S100A9 and the receptor for advanced glycation end-products (RAGE) interacts with both S100A9 and S100A4. Furthermore, we show that S100A9 and S100A4 interact with RAGE and TLR4; interactions that can be inhibited by OX. Hence, S100A4 and S100A9 display similar functional elements despite their primary sequence diversity. This was further confirmed by showing that S100A4 and S100A9 dimerize both in vitro and in vivo. All of these interactions required levels of Zn(++) that are found in the extracellular space but not intracellularly. Interestingly, S100A4 and S100A9 are expressed by distinct CD11b(+) subpopulations both in healthy animals and in animals with either inflammatory disease or tumor burden. The functions of S100A9 and S100A4 described in this paper, including heterodimerization, may therefore reflect S100A9 and S100A4 that are released into the extra-cellular milieu. (Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
PLoS ONE
volume
8
issue
5
article number
e63012
publisher
Public Library of Science
external identifiers
  • wos:000319055600052
  • pmid:23667563
  • scopus:84877298739
  • pmid:23667563
ISSN
1932-6203
DOI
10.1371/journal.pone.0063012
language
English
LU publication?
yes
id
0bd9dae9-f00c-46c8-9ac4-c4236619c069 (old id 3804554)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/23667563?dopt=Abstract
date added to LUP
2016-04-01 12:55:22
date last changed
2020-09-16 01:58:03
@article{0bd9dae9-f00c-46c8-9ac4-c4236619c069,
  abstract     = {S100A4 and S100A9 proteins have been described as playing roles in the control of tumor growth and metastasis. We show here that a chemical probe, oxyclozanide (OX), selected for inhibiting the interaction between S100A9 and the receptor for advanced glycation end-products (RAGE) interacts with both S100A9 and S100A4. Furthermore, we show that S100A9 and S100A4 interact with RAGE and TLR4; interactions that can be inhibited by OX. Hence, S100A4 and S100A9 display similar functional elements despite their primary sequence diversity. This was further confirmed by showing that S100A4 and S100A9 dimerize both in vitro and in vivo. All of these interactions required levels of Zn(++) that are found in the extracellular space but not intracellularly. Interestingly, S100A4 and S100A9 are expressed by distinct CD11b(+) subpopulations both in healthy animals and in animals with either inflammatory disease or tumor burden. The functions of S100A9 and S100A4 described in this paper, including heterodimerization, may therefore reflect S100A9 and S100A4 that are released into the extra-cellular milieu.},
  author       = {Björkman, Per and Källberg, Eva and Wellmar, Ulf and Riva, Matteo and Olsson, Anders and He, Zhifei and Törngren, Marie and Liberg, David and Ivars, Fredrik and Leanderson, Tomas},
  issn         = {1932-6203},
  language     = {eng},
  number       = {5},
  publisher    = {Public Library of Science},
  series       = {PLoS ONE},
  title        = {Common Interactions between S100A4 and S100A9 Defined by a Novel Chemical Probe.},
  url          = {https://lup.lub.lu.se/search/ws/files/3049505/4075715.pdf},
  doi          = {10.1371/journal.pone.0063012},
  volume       = {8},
  year         = {2013},
}